ID A0A0Q7BF39_9ACTN Unreviewed; 339 AA.
AC A0A0Q7BF39;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=NADPH:quinone reductase {ECO:0000313|EMBL:KQW50972.1};
GN ORFNames=ASC77_25295 {ECO:0000313|EMBL:KQW50972.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW50972.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW50972.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW50972.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW50972.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW50972.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQW50972.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMDV01000003; KQW50972.1; -; Genomic_DNA.
DR RefSeq; WP_056150619.1; NZ_LMDV01000003.1.
DR AlphaFoldDB; A0A0Q7BF39; -.
DR STRING; 1736439.ASC77_25295; -.
DR OrthoDB; 7355832at2; -.
DR Proteomes; UP000051939; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08253; zeta_crystallin; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 10..333
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 34888 MW; DB7EAB012608555C CRC64;
MRAVIYERTG GTEVLSVVHR PQPRPGPGEV LVEVAVSGVN PTDWKARRGP GELTIPQVPH
HDGAGTVKAV GPGVERPMRG DRVWLWDVAF DRPSGTAQEL VVVPAAHAVP MADAVSFDVG
ASLGIPALTA HRCLTAGLDT PEQLSESALK GRNVLVAGGA GAVGHAAIQL ASWAGAAVIS
TVSSPRKAQL AAAAGAHRVI DYSQVDVATA VRSVAPLGVD LIVEVNPSSN LALDIAVVAP
NGTIAIYASD GPDLVPFPIR AAMLKNVRTQ FVLTYTTTTS QKTAAVQSVA RAADAGVLEV
GEDAGLPLTR FPLNQTGAAH DLVQSGFTGK VLIDVPPLT
//
